Zobrazeno 1 - 6
of 6
pro vyhledávání: '"John J. Emanuele"'
Publikováno v:
Biochemistry. 36:7264-7271
Initial velocity methods were used to probe the kinetic mechanism of Escherichia coli uridine diphosphate-N-acetylmuramate:L-alanine ligase (UNAM:L-Ala ligase). When the activity (in the forward direction) versus substrate concentration data were plo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::79f6e31340a5401682216b331f024f78
https://doi.org/10.1021/bi970266r
https://doi.org/10.1021/bi970266r
Autor:
Joseph J. Villafranca, Bruce L. Jacobson, John J. Emanuele, Chiehying Y. Chang, Howard Einspahr, Haiyong Jin
Publikováno v:
Protein Science. 5:2566-2574
Uridine diphosphate-N-acetylmuramate:L-alanine ligase (EC 6.3.2.8, UNAM:L-Ala ligase or MurC gene product) catalyzes the ATP-dependent ligation of the first amino acid to the sugar moiety of the peptidoglycan precursor. This is an essential step in c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::476fa70b91f8c7fd036a86e490f0e77a
https://doi.org/10.1002/pro.5560051219
https://doi.org/10.1002/pro.5560051219
Autor:
John J. Emanuele, Paul F. Fitzpatrick
Publikováno v:
Biochemistry. 34:3716-3723
pH and kinetic isotope effects on steady-state kinetic parameters have been determined for the flavoprotein tryptophan 2-monooxygenase with tryptophan, phenylalanine, 2-hydrazino-3-propanoic acid, and methionine as substrates. The V/K values of the a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::704931db7a1ca881a21c846e642aeca0
https://doi.org/10.1021/bi00011a029
https://doi.org/10.1021/bi00011a029
Publikováno v:
Archives of Biochemistry and Biophysics. 316:241-248
Tryptophan 2-monooxygenase from Pseudomonas savastanoi is a flavoprotein which catalyzes the formation of indoleacetamide from tryptophan. This is the first step in a two-step pathway for the formation of indoleacetic acid during infection of plants
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2de9f1e00fb5168a24fd8228484599b3
https://doi.org/10.1006/abbi.1995.1034
https://doi.org/10.1006/abbi.1995.1034
Autor:
Paul Falk, Haiyong Jin, Robert Fairman, Hsu-Tso Ho, James G. Robertson, John J. Emanuele, Mark E. Hail, Joseph J. Villafranca
Publikováno v:
Biochemistry. 35(5)
Uridine diphosphate N-acetylmuramate:L-alanine ligase (EC 6.3.2.8, UNAM:L-Ala ligase or MurC gene product) adds the first amino acid to the sugar moiety of the peptidoglycan precursor, catalyzing one of the essential steps in cell wall biosynthesis f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0567e04d4599c656f610efe265f125c
https://pubmed.ncbi.nlm.nih.gov/8634272
https://pubmed.ncbi.nlm.nih.gov/8634272
Autor:
Paul F. Fitzpatrick, John J. Emanuele
Publikováno v:
Biochemistry. 34(11)
The flavoprotein tryptophan 2-monooxygenase catalyzes the oxidative decarboxylation of tryptophan to indole-3-acetamide, carbon dioxide, and water. The kinetic mechanism of the enzyme has been determined with tryptophan as substrate at pH 8.3. Initia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9b58efcc084c1e6fbf23b40be871a15
https://pubmed.ncbi.nlm.nih.gov/7893667
https://pubmed.ncbi.nlm.nih.gov/7893667